ArticleJournal of computer-aided molecular design2014
Design of a colicin E7 based chimeric zinc-finger nuclease.
Article in Journal of computer-aided molecular design, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Enhancing Production of Tryptophan via Cellulose Utilization by Escherichia coli.Applied biochemistry and biotechnology · 2026Article
- Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study.Protein science : a publication of the Protein Society · 2016Article
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6 authors.
Funding
Abstract
Colicin E7 is a natural bacterial toxin. Its nuclease domain (NColE7) enters the target cell and kills it by digesting the nucleic acids. The HNH-motif as the catalytic centre of NColE7 at the C-terminus requires the positively charged N-terminal loop for the nuclease activity-offering opportunities for allosteric control in a NColE7-based artificial nuclease. Accordingly, four novel zinc finger nucleases were designed by computational methods exploiting the special structural features of NColE7. The constructed models were subjected to MD simulations. The comparison of structural stability and functional aspects showed that these models may function as safely controlled artificial nucleases. This study was complemented by random mutagenesis experiments identifying potentially important residues for NColE7 function outside the catalytic region.
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